Abstract
The activity of Bioorganic Chemistry Group (BCG) within Department of Organic Chemistry and Technology at Budapest University of Technology and Economics is related to various areas of synthetic chemistry, biotechnology and enzymology. This review gives an overview on the research activity of the group covering development of synthetic organic chemistry methods; stereoselective biotransformations with lipases, ammonia-lyases and further biocatalysts in batch and continuous-flow reactions; novel enzyme immobilization methods; and enzyme structural and mechanistic studies by experimental and computational techniques.
Highlights
1.1 Scientific background of the Bioorganic Chemistry Research GroupThe activity of Bioorganic Chemistry Group (BCG) of Department of Organic Chemistry and Technology at Budapest University of Technology and Economics is related to various areas of synthetic chemistry, selective biocatalysis [1] and enzymology with major emphasis on development of novel tools for stereoselective synthesis [2].One of the main challenges facing organic chemistry is the rational synthesis of an ever growing number of complex, optically active natural products and their analogues [3]
The following parts of this review summarize the various activities of BCG from 2008 until recent days
The low-cost Zn dust method proved to be effective on ketones with carbonyl groups at the benzylic side-chain position of aromatic systems, whereas 10% Pd/C was an efficient catalyst even in a continuous-flow reactor for the reductive aminations of carbonyl groups non-conjugated with any π-system
Summary
Synthetic application of novel biocatalytic methods is a continuously growing area of chemistry, microbiology and genetic engineering, due to the fact that biocatalysts are selective, easy-to-handle and environmentally friendly [1,5,6] Biotransformations – catalyzed by biocatalysts – are already being used industrially to manufacture a wide range of products, including drugs, agricultural chemicals, organics, fine chemicals and plastics [7,8]. In connection to continuous-flow processes, enzyme immobilization is of primary importance because immobilized enzymes may show enhanced stability, activity and selectivity as compared to their native form. There is an extremely rapid development in understanding enzyme catalyzed processes at molecular level This enormous expansion is due to the recent developments in molecular genetics (PCR, sequencing, novel expression systems and genome projects), structural biology (protein crystallography, liquid-phase NMR protein structure determinations) and bioinformatics (protein modeling, ligand-docking and quantum chemical calculations within the active sites). The better understanding of the nature of biocatalysis can have a positive impact on the synthetic methods, or even human applications of proteins and can broaden the application of the biotransformation at novel areas [22,23,24]
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